Masaki T, Fujihashi T, Nakamura K, Soejima M
Biochim Biophys Acta. 1981 Jul 24;660(1):51-5. doi: 10.1016/0005-2744(81)90107-8.
The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates. The binding affinity of alkylamines as determined by Ki was much stronger than that of the corresponding alkylguanidines.
使用合成底物和天然底物，即赖氨酸衍生物、精氨酸衍生物、赖氨酸加压素、P物质、促肾上腺皮质激素和胰岛素，研究了无色杆菌蛋白酶I对赖氨酸残基的独特特异性。该酶仅切割上述底物中的-Lys-X-键。通过Ki测定的烷基胺的结合亲和力比相应的烷基胍强得多。
